28JS

Cryo-EM structure of the human holo-TFIIH-XPC complex bound to bulky lesion-mimic DNA (composite map)

28JS の概要

• エントリーDOI: 10.2210/pdb28js/pdb
• 関連するPDBエントリー: 28JM
• EMDBエントリー: 56544 56551
• 分子名称: General transcription and DNA repair factor IIH helicase subunit XPB, Lysine-specific demethylase RAD23B, Centrin-2, ... (16 entities in total)
• 機能のキーワード: nucleotide excision repair, dna repair, helicase, transcription factor, dna binding protein
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 13
• 化学式量合計: 641643.69

構造登録者

de Martin Garrido, N.,Haste, C.A.F.,Feng, J.,Cronin, N.B.,Greber, B.J. (登録日: 2026-02-03, 公開日: 2026-05-06, 最終更新日: 2026-09-02)

主引用文献

de Martin Garrido, N.,Haste, C.A.F.,Feng, J.,Cronin, N.B.,Greber, B.J.
Visualization of stepwise derepression of TFIIH in global genome nucleotide excision repair.
Sci Adv, 12:eaeb3506-eaeb3506, 2026

PubMed Abstract: Nucleotide excision repair (NER) is a crucial DNA repair pathway that is orchestrated by transcription factor IIH (TFIIH) in eukaryotic cells. TFIIH is a multifunctional complex that contains two DNA helicase/DNA translocase subunits and a kinase module, different subsets of which act in NER, transcription initiation, and cell cycle control. To ensure fidelity despite multifunctionality, the DNA helicase activity of TFIIH is autoinhibited in its free form or when the factor engages in transcription initiation. While the release of the kinase module has been identified as a key step in TFIIH activation, the molecular mechanisms controlling this step and concomitant structural changes in TFIIH are incompletely understood. Here, we determine high-resolution structures of three NER intermediates that visualize how TFIIH arrives at sites of DNA damage in an autoinhibited state and how autoinhibition is released via previously undescribed intermediates. These findings contribute to a mechanistic understanding of human DNA repair.

PubMed: 42490432
DOI: 10.1126/sciadv.aeb3506

実験手法

ELECTRON MICROSCOPY (3.32 Å)